1PIN

PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0001666	biological_process	response to hypoxia
A	0001934	biological_process	positive regulation of protein phosphorylation
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0003774	molecular_function	cytoskeletal motor activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006626	biological_process	protein targeting to mitochondrion
A	0007088	biological_process	regulation of mitotic nuclear division
A	0007266	biological_process	Rho protein signal transduction
A	0008013	molecular_function	beta-catenin binding
A	0010468	biological_process	regulation of gene expression
A	0016607	cellular_component	nuclear speck
A	0016853	molecular_function	isomerase activity
A	0016859	molecular_function	cis-trans isomerase activity
A	0030182	biological_process	neuron differentiation
A	0030496	cellular_component	midbody
A	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
A	0031434	molecular_function	mitogen-activated protein kinase kinase binding
A	0031647	biological_process	regulation of protein stability
A	0031648	biological_process	protein destabilization
A	0032465	biological_process	regulation of cytokinesis
A	0032794	molecular_function	GTPase activating protein binding
A	0036064	cellular_component	ciliary basal body
A	0042177	biological_process	negative regulation of protein catabolic process
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046785	biological_process	microtubule polymerization
A	0048156	molecular_function	tau protein binding
A	0050808	biological_process	synapse organization
A	0050815	molecular_function	phosphoserine residue binding
A	0050816	molecular_function	phosphothreonine residue binding
A	0050821	biological_process	protein stabilization
A	0051219	molecular_function	phosphoprotein binding
A	0060392	biological_process	negative regulation of SMAD protein signal transduction
A	0070373	biological_process	negative regulation of ERK1 and ERK2 cascade
A	0071456	biological_process	cellular response to hypoxia
A	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
A	0098978	cellular_component	glutamatergic synapse
A	0099524	cellular_component	postsynaptic cytosol
A	1900180	biological_process	regulation of protein localization to nucleus
A	1902430	biological_process	negative regulation of amyloid-beta formation
A	1903444	biological_process	negative regulation of brown fat cell differentiation
A	1990757	molecular_function	ubiquitin ligase activator activity
A	2000146	biological_process	negative regulation of cell motility

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ALA A 201

Chain	Residue
A	PRO202
A	HOH1113

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PRO A 202

Chain	Residue
A	HOH1141
A	HOH1142
A	LEU122
A	GLN129
A	MET130
A	ALA201

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 400

Chain	Residue
A	LYS63
A	ARG68
A	ARG69
A	SER154
A	HOH1113

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 1PG A 300

Chain	Residue
A	TYR23
A	SER32
A	GLN33
A	TRP34
A	LYS97
A	HOH1020
A	HOH1036
A	HOH1116
A	HOH1163

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE 1PG A 301

Chain	Residue
A	HOH1198

---

site_id	ACT
Number of Residues	3
Details	THE ACTIVE SITE OF THE PPIASE DOMAIN IS MARKED BY THE BOUND ALA-PRO DIPEPTIDE (CHAIN B).

Chain	Residue
A	HIS59
A	CYS113
A	HIS157

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Functional Information from PROSITE/UniProt

site_id	PS01096
Number of Residues	21
Details	PPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEsLAsqfSdcs.Saka..RGdLG

Chain	Residue	Details
A	PHE103-GLY123

---

site_id	PS01159
Number of Residues	27
Details	WW_DOMAIN_1 WW/rsp5/WWP domain signature. WekrmsrssgrvYYfnhitnaSQWERP

Chain	Residue	Details
A	TRP11-PRO37

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	111
Details	Domain: {"description":"PpiC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00278","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"PubMed","id":"21497122","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29686383","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1nmw

Chain	Residue	Details
A	CYS113
A	HIS59
A	HIS157

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 511

Chain	Residue	Details
A	HIS59	proton shuttle (general acid/base)
A	CYS113	covalently attached, electrostatic stabiliser
A	GLN131	electrostatic stabiliser
A	SER154	electrostatic stabiliser
A	HIS157	electrostatic stabiliser

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